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Journal Article

In situ structural analysis of Golgi intracisternal protein arrays

MPS-Authors
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Engel,  Benjamin D.
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Schaffer,  Miroslava
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Albert,  Sahradha
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons77681

Asano,  Shoh
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Plitzko,  Jürgen M.
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

/persons/resource/persons77721

Baumeister,  Wolfgang
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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http://www.pnas.org/lookup/suppl/doi:10.1073/pnas.1515337112/-/DCSupplemental
(Supplementary material)

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Fulltext (public)

11264.full.pdf
(Publisher version), 3MB

Supplementary Material (public)

pnas.201515337SI.pdf
(Supplementary material), 485KB

Citation

Engel, B. D., Schaffer, M., Albert, S., Asano, S., Plitzko, J. M., & Baumeister, W. (2015). In situ structural analysis of Golgi intracisternal protein arrays. Proceedings of the National Academy of Sciences of the United States of America, 112(36), 11264-11269. doi:10.1073/pnas.1515337112.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0028-9524-B
Abstract
We acquired molecular-resolution structures of the Golgi within its native cellular environment. Vitreous Chlamydomonas cells were thinned by cryo-focused ion beam milling and then visualized by cryo-electron tomography. These tomograms revealed structures within the Golgi cisternae that have not been seen before. Narrow trans-Golgi lumina were spanned by asymmetric membrane-associated protein arrays that had similar to 6-nm lateral periodicity. Subtomogram averaging showed that the arrays may determine the narrow central spacing of the trans-Golgi cisternae through zipper-like interactions, thereby forcing cargo to the trans-Golgi periphery. Additionally, we observed dense granular aggregates within cisternae and intracisternal filament bundles associated with trans-Golgi buds. These native in situ structures provide new molecular insights into Golgi architecture and function.